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B p50-Dependent In Vivo Footprints at Ig S
3 DNA Are Correlated with µ
3 Switch Recombination1
Department of Microbiology and Immunology, University of Illinois College of Medicine, Chicago, IL 60680
NF-
B has been demonstrated to play critical roles in multiple
aspects of immune responses including Ig H chain isotype switching. To
better define the specific roles the p50 subunit of NF-B plays in
µ
3 switch recombination (SR), we systematically evaluated
p50-deficient B cells for activities that are strongly correlated with
SR. B cell activation with LPS plus anti-IgD-dextran plus IL-5 plus
IL-4 plus TGF-
produced normal levels of proliferation and 3
germline transcripts in p50-deficient B cells, but µ3 SR was
impaired. In vitro binding studies previously showed that NF-B p50
homodimer binds the switch nuclear B-site protein (SNIP) of the S3
tandem repeat. Ligation-mediated PCR in vivo footprint analysis
demonstrates that the region spanning the SNIP and switch nuclear
A-site protein (SNAP) binding sites of the S3 region are contacted
by protein in normal resting splenic B cells. B cells that are
homozygous for the targeted disruption of the gene encoding p50 (-/-)
show strong aberrant footprints, whereas heterozygous cells (+/-)
reveal a partial effect in S3 DNA. These studies provide evidence of
nucleoprotein interactions at switch DNA in vivo and suggest a direct
interaction of p50 with S3 DNA that is strongly correlated with SR
competence.
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